Table 2.
Crystallographic data collection and refinement statistics for MATα2 mutants
| Mutants | S114A | S114A | R264A |
|---|---|---|---|
| Data collection | |||
| Space group | P22121 | I222 | I222 |
| Cell dimensions | |||
| a, b, c (Å) | 62.09, 102.87, 108.17 | 66.62, 94.68, 116.55 | 67.14, 94.23, 116.82 |
| α, β, ϒ (Å) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution (Å) | 54.08–1.65 | 58.28–1.80 | 58.41–1.70 |
| (last shell) (Å) | (1.68–1.65) | (1.84–1.80) | (1.73–1.70) |
| No. of reflections | 81 704 | 34 507 | 40 576 |
| R merge (%) | 10.8 (56.6) | 17.0 (76.6) | 12.4 (51.3) |
| I/Ϭ I | 8.0 (1.9) | 5.80 (2.0) | 5.9 (1.9) |
| Completeness (%) | 97.2 (98.4) | 99.8 (100) | 98.7 (99.8) |
| Redundancy | 5.3 (5.3) | 5.3 (5.4) | 4.3 (4.1) |
| Wilson B factor (Å2) | 14.90 | 17.10 | 12.40 |
| Refinement | |||
| R work/R free** | 16.32/19.46 | 15.10/17.44 | 16.00/18.42 |
| No. of atoms | |||
| Protein | 5902 | 3005 | 2963 |
| Ligand | 78 | 79 | 66 |
| Waters | 499 | 224 | 284 |
| Average B‐factors (Å2) | |||
| Protein | 21.72 | 15.30 | 15.30 |
| Ligand | 27.77 | 32.78 | 21.77 |
| Water | 27.77 | 24.81 | 29.36 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.015 | 0.014 | 0.015 |
| Bond angles (°) | 1.760 | 1.670 | 1.695 |
| PDB Code | http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6FBP | http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6FBO | http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6FCD |